메뉴 건너뛰기




Volumn 276, Issue 2, 1998, Pages 437-448

Rice non-specific lipid transfer protein: The 1.6 Å crystal structure in the unliganded state reveals a small hydrophobic cavity

Author keywords

Crystal structure; Hydrophobic cavity; Non specific lipid transfer protein; Probable amylase protease inhibitor; Rice protein

Indexed keywords

STEROL CARRIER PROTEIN 2; SULFATE; SULFONIC ACID DERIVATIVE; VEGETABLE PROTEIN; WATER;

EID: 0032548996     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1550     Document Type: Article
Times cited : (124)

References (50)
  • 1
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 2
    • 0027202271 scopus 로고
    • Crystal structure of hydrophobic protein from soybean: A member of a new cysteine-rich family
    • Baud F., Pebay-Peyroula E., Cohen-Addad C., Odani S., Lehmann M.S. Crystal structure of hydrophobic protein from soybean a member of a new cysteine-rich family. J. Mol. Biol. 231:1993;877-887
    • (1993) J. Mol. Biol. , vol.231 , pp. 877-887
    • Baud, F.1    Pebay-Peyroula, E.2    Cohen-Addad, C.3    Odani, S.4    Lehmann, M.S.5
  • 3
    • 0024507401 scopus 로고
    • Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology
    • Bernhard W.R., Somerville C.R. Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology. Arch. Biochem. Biophys. 269:1989;695-697
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 695-697
    • Bernhard, W.R.1    Somerville, C.R.2
  • 6
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 7
    • 0003786944 scopus 로고
    • The complete amino acid sequence of the α-amylase inhibitor I-2 from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.)
    • Campos F.A.P., Richardson M. The complete amino acid sequence of the α-amylase inhibitor I-2 from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.). FEBS Letters. 167:1984;221-225
    • (1984) FEBS Letters , vol.167 , pp. 221-225
    • Campos, F.A.P.1    Richardson, M.2
  • 8
    • 0026852571 scopus 로고
    • Fast rigid-body refinement for molecular-replacement techniques
    • Castellano E.E., Oliva G., Navaza J. Fast rigid-body refinement for molecular-replacement techniques. J. Appl. Crystallog. 25:1992;281-284
    • (1992) J. Appl. Crystallog. , vol.25 , pp. 281-284
    • Castellano, E.E.1    Oliva, G.2    Navaza, J.3
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 10
    • 0000007118 scopus 로고
    • Purification of a basic phospholipid transfer protein from maize seedlings
    • Douady D., Grosbois M., Guerbette F., Kader J. Purification of a basic phospholipid transfer protein from maize seedlings. Biochim. Biophys. Acta. 710:1982;143-153
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 143-153
    • Douady, D.1    Grosbois, M.2    Guerbette, F.3    Kader, J.4
  • 11
    • 0000330090 scopus 로고
    • Purification of phospholipid transfer protein from seeds using a two-step chromatographic procedure
    • Douady D., Guerbette F., Kader J. Purification of phospholipid transfer protein from seeds using a two-step chromatographic procedure. Physiol. Veg. 23:1985;373-380
    • (1985) Physiol. Veg. , vol.23 , pp. 373-380
    • Douady, D.1    Guerbette, F.2    Kader, J.3
  • 12
    • 0027949791 scopus 로고
    • Lipid transfer protein genes specifically expressed in barley leaves and coleoptiles
    • Gausing K. Lipid transfer protein genes specifically expressed in barley leaves and coleoptiles. Planta. 192:1994;574-580
    • (1994) Planta , vol.192 , pp. 574-580
    • Gausing, K.1
  • 14
    • 0030005766 scopus 로고    scopus 로고
    • Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds
    • Gomar J., Petit M.C., Sodano P., Sy D., Marion D., Kader J.C., Vovelle F., Ptak M. Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds. Protein Sci. 5:1996;565-577
    • (1996) Protein Sci. , vol.5 , pp. 565-577
    • Gomar, J.1    Petit, M.C.2    Sodano, P.3    Sy, D.4    Marion, D.5    Kader, J.C.6    Vovelle, F.7    Ptak, M.8
  • 16
    • 0027508876 scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds
    • Hwang K.Y., Kim K.K., Min K., Eom S.H., Yu Y.G., Kim S., Sweet R.M., Suh S.W. Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds. J. Mol. Biol. 229:1993;255-257
    • (1993) J. Mol. Biol. , vol.229 , pp. 255-257
    • Hwang, K.Y.1    Kim, K.K.2    Min, K.3    Eom, S.H.4    Yu, Y.G.5    Kim, S.6    Sweet, R.M.7    Suh, S.W.8
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21:1988;916-924
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 20
    • 0021402150 scopus 로고
    • Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts
    • Kader J.C., Julienne M., Vergnolle C. Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts. Eur. J. Biochem. 139:1984;411-416
    • (1984) Eur. J. Biochem. , vol.139 , pp. 411-416
    • Kader, J.C.1    Julienne, M.2    Vergnolle, C.3
  • 21
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G.J., Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog. sect. D. 50:1994;178-185
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 22
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0031568810 scopus 로고    scopus 로고
    • Barley lipid-transfer protein complexed with palmitoyl CoA: The structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands
    • Lerche M.H., Kragelund B.B., Bech L.M., Poulsen F.M. Barley lipid-transfer protein complexed with palmitoyl CoA the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands. Structure. 5:1997;291-306
    • (1997) Structure , vol.5 , pp. 291-306
    • Lerche, M.H.1    Kragelund, B.B.2    Bech, L.M.3    Poulsen, F.M.4
  • 26
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determinationn des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la determinationn des structures cristallines. Acta Crystallog. 5:1952;802-810
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 27
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 29
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography
    • Messerschmidt A., Pflugrath J.W. Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Crystallog. 20:1987;306-315
    • (1987) J. Appl. Crystallog. , vol.20 , pp. 306-315
    • Messerschmidt, A.1    Pflugrath, J.W.2
  • 30
    • 0027722868 scopus 로고
    • Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins
    • Molina A., Garcia-Olmedo F. Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins. Plant J. 4:1993;983-991
    • (1993) Plant J. , vol.4 , pp. 983-991
    • Molina, A.1    Garcia-Olmedo, F.2
  • 31
    • 0027507001 scopus 로고
    • Lipid transfer proteins (nsLTPs) from barley and leaves are potent inhibitors of bacterial and fungal plant pathogens
    • Molina A., Segura A., Garcia-Olmedo F. Lipid transfer proteins (nsLTPs) from barley and leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Letters. 316:1993;119-122
    • (1993) FEBS Letters , vol.316 , pp. 119-122
    • Molina, A.1    Segura, A.2    Garcia-Olmedo, F.3
  • 32
    • 0002468465 scopus 로고
    • Selective expression of a probable amylase/protein inhibitor in barley aleurone cells: Comparison to the barley amylase/subtilisin inhibitor
    • Mundy J., Rogers J.C. Selective expression of a probable amylase/protein inhibitor in barley aleurone cells Comparison to the barley amylase/subtilisin inhibitor. Planta. 169:1986;51-63
    • (1986) Planta , vol.169 , pp. 51-63
    • Mundy, J.1    Rogers, J.C.2
  • 33
    • 0000997620 scopus 로고
    • On the computation of the fast rotation function
    • Navaza J. On the computation of the fast rotation function. Acta Crystallog. sect. D. 49:1993;588-591
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 588-591
    • Navaza, J.1
  • 34
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman S.B., Wunsch C.D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:1970;443-453
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 36
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls A., Bharadwaj R., Honig B. GRASP graphical representation and analysis of surface properties. Biophys. J. 64:1993;166-170
    • (1993) Biophys. J. , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 38
    • 0028363877 scopus 로고
    • Identification of a lipid transfer protein as the major protein in the surface wax of broccoli leaves
    • Pyee J., Yu H., Kolattukudy P.E. Identification of a lipid transfer protein as the major protein in the surface wax of broccoli leaves. Arch. Biochem. Biophys. 331:1994;460-468
    • (1994) Arch. Biochem. Biophys. , vol.331 , pp. 460-468
    • Pyee, J.1    Yu, H.2    Kolattukudy, P.E.3
  • 39
    • 0000082544 scopus 로고
    • CHAIN: A crystallographic modeling program
    • Sack J.S. CHAIN a crystallographic modeling program. J. Mol. Graph. 6:1988;244-245
    • (1988) J. Mol. Graph. , vol.6 , pp. 244-245
    • Sack, J.S.1
  • 40
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 41
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., Suh S.W. High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure. 3:1995;189-199
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 42
    • 0026357569 scopus 로고
    • 1H NMR studies of a wheat phospholipid transfer protein: Sequential resonance assignments and secondary structure
    • 1H NMR studies of a wheat phospholipid transfer protein sequential resonance assignments and secondary structure. Biochemistry. 30:1991;11600-11608
    • (1991) Biochemistry , vol.30 , pp. 11600-11608
    • Simorre, J.P.1    Caille, A.2    Marion, D.3    Marion, D.4    Ptak, M.5
  • 45
    • 0000690996 scopus 로고
    • The amino-acid sequence of the nonspecific lipid transfer protein from germinated caster bean endosperms
    • Takishima K., Watanabe S., Yamada M., Mamiya G. The amino-acid sequence of the nonspecific lipid transfer protein from germinated caster bean endosperms. Biochim. Biophys. Acta. 870:1986;248-255
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 248-255
    • Takishima, K.1    Watanabe, S.2    Yamada, M.3    Mamiya, G.4
  • 46
    • 0001469527 scopus 로고
    • In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologus to nonspecific lipid transfer proteins
    • Terras F.R.G., Goderis I.J., Van Leuvren F., Vanderleyden J., Cammue B.P.A., Broekaert W.F. In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologus to nonspecific lipid transfer proteins. Plant Physiol. 100:1992;1055-1058
    • (1992) Plant Physiol. , vol.100 , pp. 1055-1058
    • Terras, F.R.G.1    Goderis, I.J.2    Van Leuvren, F.3    Vanderleyden, J.4    Cammue, B.P.A.5    Broekaert, W.F.6
  • 47
    • 0026554314 scopus 로고
    • Nonspecific lipid transfer protein in castor bean cotyledon cells: Subcellular localization and a possible role in lipid metabolism
    • Tsuboi S., Osafune T., Nishimura M., Yamada M. Nonspecific lipid transfer protein in castor bean cotyledon cells Subcellular localization and a possible role in lipid metabolism. J. Biochem. 111:1992;500-508
    • (1992) J. Biochem. , vol.111 , pp. 500-508
    • Tsuboi, S.1    Osafune, T.2    Nishimura, M.3    Yamada, M.4
  • 49
    • 0002863521 scopus 로고
    • Strategies for extracting isomorphous and anomalous signals
    • D. Sayre. Oxford: Oxford University Press (Clarendon)
    • Weissmann L. Strategies for extracting isomorphous and anomalous signals. Sayre D. Computational Crystallography. 1982;56-63 Oxford University Press (Clarendon), Oxford
    • (1982) Computational Crystallography , pp. 56-63
    • Weissmann, L.1
  • 50
    • 0024075865 scopus 로고
    • Amino acid sequence of a probable amylase/protease inhibitor from rice seeds
    • Yu Y.G., Chung C.H., Fowler A., Suh S.W. Amino acid sequence of a probable amylase/protease inhibitor from rice seeds. Arch. Biochem. Biophys. 265:1988;465-475
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 465-475
    • Yu, Y.G.1    Chung, C.H.2    Fowler, A.3    Suh, S.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.